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. 2002 Apr;68(4):1658–1664. doi: 10.1128/AEM.68.4.1658-1664.2002

TABLE 1.

Comparison of specificities of various amylolytic enzymes

Substrate Initial velocitya
NPL CDase BLMA BMNP BSA BLA NOV β-AMY
Potato amylose 100.0 100.0 100.0 100.0 100.0 100.0 100.0 100.0
Amylose AS-1000 114.3 122.9 140.6 106.6 116.5 95.5 66.1 14.9
Amylose AS-320 106.1 130.2 130.4 96.6 101.9 82.0 64.6 26.4
Amylose AS-110 119.8 148.6 154.6 89.1 106.6 85.3 65.0 65.8
Amylose AS-70 133.1 155.4 153.0 89.8 112.1 90.1 65.4 98.0
Amylose EX-III 161.7 212.0 232.6 85.1 107.9 85.8 89.8 138.6
Amylose EX-I 194.2 265.6 261.7 60.3 66.6 56.5 80.5 143.6
Maltoheptaose 117.1 173.1 291.0 23.8 19.6 44.7 67.1 38.0
Maltohexaose 115.3 141.5 254.3 23.5 22.2 13.9 64.3 42.6
Maltopentaose 107.0 178.1 246.1 13.6 13.3 8.2 61.1 29.6
Maltotetraose 67.4 87.9 171.4 14.6 8.6 11.2 35.2 22.5
Maltotriose 24.9 69.9 46.7 NDb ND ND 22.6 ND
Potato amylopectin ND ND ND 74.9 83.5 76.4 115.9 85.9
Waxy maize starch ND ND ND 61.9 76.5 78.6 129.6 114.2
Higly branched cyclic dextrin 14.9 ND ND 57.7 74.2 70.0 127.1 98.5
Potato starch 31.9 10.8 26.0 59.5 77.2 66.5 92.5 62.4
α-Cyclomaltodextrin 413.7 400.5 568.9 ND ND ND ND ND
β-Cyclomaltodextrin 401.8 481.6 449.8 18.2 ND ND ND ND
γ-Cyclomaltodextrin 379.9 596.7 526.4 53.8 55.3 ND ND ND
Pullulan 59.0 7.0 ND 9.5 ND ND ND ND
a

The initial velocity is indicated with respect to that for potato amylose, which was defined as 100. NPL, B. stearothermophilus neopullulanase; CDase, cyclomaltodextrinase; BLMA, B. licheniformis maltogenic amylase; BMNP, B. megaterium neopullulanase; BSA, bacterial saccharifing α-amylase; BLA, bacterial liquefying α-amylase; NOV, Novamyl; β-AMY, soybean β-amylase.

b

ND, enzyme activity was not detectable (the initial velocity was less than 1/100 of that for potato amylose).